2NMY
Crystal structure analysis of HIV-1 protease mutant V82A with a inhibitor saquinavir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2004-11-11 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 59.988, 87.464, 47.190 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.100 |
R-factor | 0.1491 |
Rwork | 0.149 |
R-free | 0.18130 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 0.045 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.140 |
High resolution limit [Å] | 1.100 | 1.100 |
Rmerge | 0.110 | 0.360 |
Number of reflections | 95683 | |
<I/σ(I)> | 10.5 | 2 |
Completeness [%] | 94.6 | 64.5 |
Redundancy | 4.7 | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | SODIUM CHLORIDE 0.6M, DMSO 10%, SODIUM ACETATE BUFFER PH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |